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Home > Mathematics and Science Textbooks > Biology, life sciences > Functional Genomic Analysis of Mucin Secretion in Airway Epithelial Cells
Functional Genomic Analysis of Mucin Secretion in Airway Epithelial Cells

Functional Genomic Analysis of Mucin Secretion in Airway Epithelial Cells


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About the Book

Mucin secretion in the airways is an exocytotic event that can cause substantial problems when it is imbalanced. Disproportionately large levels of mucin secretion can lead to impaired mucociliary function, increased susceptibility to bacterial pathogens, enhanced of inflammatory responses due to increases in inflammatory mediators and enzymes that induce MUC gene expression, mucin synthesis, and goblet cell hyperplasia, and, in extreme cases, death. The process of regulated exocytosis in the airway epithelium is still poorly understood, eventhough the results of an aberrent process are potentially so deleterious. Previous studies from our lab demonstrated that Myristoylated Alanine-Rich C Kinase substrate protein (MARCKS) regulated mucin secretion in in vitro cultures of human bronchial epithelial cells and in mice in vivo. It is our hypothesis that MARCKS mediates the exocytotic release of mucin from preformed membrane-bound mucin granules by facilitating granule movement from the cytosol to the plasma membrane where the granule docks, fuses and secretes its contents into the airway lumen. In these studies, we use proteomics to elucidate novel proteins involved in mucin secretion that are associated with the mucin granules in the secretory cells. These studies will greatly contribute to our understanding of proteins involved in regulated exocytosis, suggesting new therapeutic targets. In the first study, we elucidate some aspects of the regulated exocytosis mechanism whereby MARCKS, hCLCA1, and the chaperones cysteine string protein and heat shock proteins interact in a complex. We found that these proteins form a complex that is associated with the mucin granule in normal bronchial epithelial cells grown using the in vitro air-liquid interface culture system. We further elucidated novel proteins that also associate with the mucin granule, most of which are cytoskeletal related. The second study elucidates proteins associated with the mucin granules in unstimulated and stimulated conditions further expanding the study to include a diseased cystic fibrosis model and an intestinal cell line. We found that many proteins are conserved across these cell types, suggesting possible conservation in the regulated exocytosis machinery involved in mucin secretion.


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Product Details
  • ISBN-13: 9781244022119
  • Publisher: Proquest, Umi Dissertation Publishing
  • Publisher Imprint: Proquest, Umi Dissertation Publishing
  • Height: 254 mm
  • Weight: 313 gr
  • ISBN-10: 124402211X
  • Publisher Date: 01 Sep 2011
  • Binding: Paperback
  • Spine Width: 10 mm
  • Width: 203 mm


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Functional Genomic Analysis of Mucin Secretion in Airway Epithelial Cells
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